COMPOSITION OF LECTIN RECEPTORS IN SEROUS AND MUCINOUS OVARIAN CYSTADENOMAS

The most common group of benign cystic ovarian tumors in women of all ages are epithelial tumors (cystadenomas) that make up about a third of ovarian tumors and half of benign lesions. The growth of tumor proliferative activity accompanied by increased number of lectins receptors in cells. Lectins are non-immune origin proteins that have a common property of binding carbohydrates and carbohydrate determinants of biopolymers strictly defined structure and intact their covalent structure. It was established that oncogenesis changes of the structure of glycoconjugates membrane as cancer and immune cells, and mark faster than glycoconjugates variability in tumor cells. This is the basis for the use of labeled lectins to study changes in cell membrane and secretory structures of glycoconjugates during tumor growth. The aim of the study was to determine the composition of the receptors in serous and mucinous cystadenomas. Operating material was studied from 60 women operated on for ovarian serous cystadenomas, and from 60 patients – on for ovarian mucinous cystadenomas. To identify the set of glycoconjugates it were used peroxidaselabeled lectins with different carbohydrate specificity. Characteristic of serous and mucinous cystadenomas was the accumulation of lectins receptors in their cells of wheat germs (WGA), groundnut seed (PNA) and soybean seeds (SBA). Papillary serous cystadenomas differed moderate accumulation in the epithelium papillae throughout the cytoplasm lectins receptors of SBA, mistletoe (VAL) and WGA. The most intense and uniform expression in mucinous cystadenomas was one of lectin receptors of bark elderberry (SNA) and SBA. The authors conclude that changes in the molecular-spatial structure of glycoconjugates of the plasmolemma cells surfaces and increase of the mobility of membrane lectins receptors in serous and mucinous cystadenomas cause lack of contact inhibition of proliferation. In their opinion, further study of lectins can contribute to the elucidation of the pathogenesis of ovarian formations, their differential diagnosis, the development of tumor markers and drugs lectins.


INTRODUCTION
Ovarian tumors take 2nd place among all genital formations and the 2-3rd place in the structure of emergency gynecological pathology.Over the past two decades the frequency of their occurrence among of gynecological patients increased from 6-11% to 19-25%.75-87% of all ovarian tumors are benign [1].The most common group of benign cystic ovarian tumors in women of all ages are cystic epithelial tumors, which make up about a third of ovarian tumors and half of its his benign formations.Histogenesis of true benign ovarian tumors, despite the many years of studying history, remains unexplored [1].

ANALYSIS OF PUBLISHED DATA AND FORMULATION OF RESEARCH TASK
The growth of tumor proliferative activity is accompanied by increased amounts of lectins receptors in cells [2].Lectins are proteins of non-immune origin who own common property to bind carbohydrates and carbohydrate determinants biopolymers strictly defined structure intact their covalent structure, and in some cases -with some subpopulations consisting unrecognized by other grounds morpho-and hystogenetic features cellular elements [3,4].
The structure of the tumor antigens are carbon structures of membrane glycoproteins, glycolipids and polysaccharides.Glycoproteins are ~ 80% proteins located on the cell surface and in the extracellular environment.They participate in the growth and adhesion of cells, control of immune responses, regulation of proteins transport and signaling pathways such as Notch, Wnt, transforming growth factor β and other [5][6][7].
It was established that the oncogenesis changes the structure of membrane glycoconjugates as well cancer as immune cells, and it was marked the advancing variability of glycoconjugates in tumor cells These changes are associated with violation of specific glycosyltransferases synthesis [8].Glycans changes are not necessarily a consequence of mutations and deletions at the DNA level of corresponding glycosyltransferases, but rather it may be caused by epigenetic modifications of DNA such as hyperor hipomethylation that regulate the expression of the variable genes [9,10].
Everything listed above is the basis for the use of labeled lectins to study changes in cell membrane and secretory glycoconjugates structures during tumor growth.
The aim of the study was to determine the receptor of lectins and their carbohydrate determinants in serous and mucinous cystadenomas.

MATERIALS AND METHODS
120 operated patients of reproductive age were under observation.Group C was 60 women with ovarian serous cystadenomas; Group M -60 women with mucinous cystadenomas.The diagnosis was confirmed histologically.
Sections 4-5 microns thick were studied using light microscope Olympus BX-40.Digital photography apparatus carried C200 ZOOM Olympus Dp-Soft.Statistical analysis of the data was performed using Microsoft Excel.

RESULTS AND DISCUSSION
The average age of women with serous cystadenomas was 30.10 ± 0.51 years, with mucinous cystadenomas -30.17 ± 0.47 and didn't significantly differ between groups.The average diameter of serous cystadenomas equal to 9.06 ± 0.60 cm, mucinous -11.97 ± 0.81 cm.
Characteristic of serous and mucinous cystadenomas was the accumulation of lectins receptors WGA, PNA and SBA in their cells (Fig. 1-3).
Peanut lectin (PNA) interacts with the T-antigen and related structures with terminal molecule of D-galactose to N-linked acethylglucosamine and ASIA-GM1 tetracarbohydrate.Wheat germ lectin (WGA) connects dicarbohydrate neuraminic-N-acidacethylglucosamine (NeuAc-NAcGlc-R) and soybean lectin (SBA) -α-methyl-N-acetyl-B-galactosamine (GalNAc-α) and oligosaccharide residues with terminal molecules GalNAc-α.Lectins PNA, WGA and SBA have cytotoxic effects and inhibit cell adhesion [11].Among receptor glycoconjugates in the epithelium of some serous cystadenomas largest content was receptors PNA and WGA.Papillary serous cystadenomas differed moderate accumulation in the epithelium of papillae throughout the cytoplasm lectin receptors SBA, VAL (Fig. 4) and WGA (Fig. 1B).17 For mucinous cystadenomas it was typical the accumulation of glycoconjugates in epithelial lining.The most intense and uniform in mucinous cystadenomas was expression of lectin receptor SNA, binding neuraminic acid, and SBA (Fig. 5).Also, there was an intense mosaic expression of receptors PNA, WGA, LAL, LCA, HPA.
Appearance receptor PNA, SBA, HPA cells in serous and mucinous cystadenomas can explain by violation of the processes of the final glycosylation of biopolymers containing carbohydrates, namely, the lack of camouflage terminal residues of D-galactose sialic acid.These violations of final glycosylation of lectins receptors in serous and mucinous cystadenomas are manifestations of sharply reduced general ability of tumor cells to produce glycolipids and glycoproteins with fully synthesized oligosaccharides chain.
The hypersialylation of epithelial cells of serous and mucinous cystadenomas, accompanied by the accumulation of receptors WGA and SNA, shows a decline in cell differentiation.Usually in hypersialylational cells there is no accumulation of fucoconjugates.Characteristic features of mucinous cells were simultaneous presence fuco-and sialoconjugates.
Mosaic lectin receptor expression may explain the formation of local condensable of receptors in certain areas of plasmolemma due to changes molecular spatial structure glycoconjugates plasmolemma surface of tumor cells and increasing the mobility of membrane receptors of lectins that keeping-phenomenon.The combination of the above composition and properties of surface glycoconjugates causes lack of contact inhibition of cell proliferation -the cardinal signs of tumor cells.
In cell adhesion fucolihandes of membrane glycoconjugates are also important.In the studied formations it was observed absence of the low content fucolihandes, in some mucinous cystadenomas -moderate content, indicating the presence of tumor properties of these entities.Reducing the strength of the surface glycoconjugates, synthesized by formations cells, hypersialylation of epithelial surfaces of cystadenomas leads to lower recognition by mononuclear phagocytes system, prevents elimination of cells by the immune system and, consequently, to persistence.
Increased affinity for lectins can be caused by a decrease in the degree of intercellular communication and detection of carbohydrate determinants of cytolemma outer layer that enables penetration of lectins in the middle of the cell and settling their respective carbohydrate fragments in the cytosol.Increasing the number of receptors explains the incompleteness of the final glycosylation lectins receptors, therefore metabolism violation in tumor cells.

CONCLUSION
Changes in the molecular-spatial structure of glycoconjugates of the plasmolemma cells surfaces and increase of the mobility of membrane lectins receptors in serous and mucinous cystadenomas cause lack of contact inhibition of proliferation.Further study of lectins can contribute to the elucidation of the pathogenesis of ovarian formations, their differential diagnosis, the development of tumor markers and drugs lectins.Processing of cuts by mistletoe lectin with peroxidase.Magnification × 400.

А В FIGURE 5. THE HIGH CONTENT OF ELDERBERRY LECTIN RECEPTORS (SNA) IN THE EPITHELIUM SMOOTH-WALLED (A) AND PAPILLARY (B) MUCINOUS CYSTADENOMAS
Processing of cuts by elderberry lectin with peroxidase.Magnification × 400.

FIGURE 1 .
FIGURE 1. UNEVEN, MODERATE TO HIGH ACCUMULATION of wheat lectin receptors (WGA) in epithelium of mucinous (A) and serous (B) cystadenomas.Processing of cuts by wheat lectin with peroxidase.Magnification × 400.

FIGURE 3 .
FIGURE 3. UNEVEN MODERATE ACCUMULATIONof soybean lectin receptors (SBA) in the cytoplasm of epithelial cells of mucinous cystadenoma (A, magnification × 100) and apical part of epithelial cells papillary serous cystadenoma (B, magnification × 400).Processing of cuts by soybean lectin with peroxidase.